ID D3P154_AZOS1 Unreviewed; 766 AA.
AC D3P154;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating)(NADP+) {ECO:0000313|EMBL:BAI74383.1};
DE EC=1.1.1.40 {ECO:0000313|EMBL:BAI74383.1};
GN Name=maeB {ECO:0000313|EMBL:BAI74383.1};
GN OrderedLocusNames=AZL_a08520 {ECO:0000313|EMBL:BAI74383.1};
OS Azospirillum sp. (strain B510).
OG Plasmid pAB510a {ECO:0000313|EMBL:BAI74383.1,
OG ECO:0000313|Proteomes:UP000002040}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI74383.1, ECO:0000313|Proteomes:UP000002040};
RN [1] {ECO:0000313|EMBL:BAI74383.1, ECO:0000313|Proteomes:UP000002040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B510 {ECO:0000313|EMBL:BAI74383.1,
RC ECO:0000313|Proteomes:UP000002040};
RC PLASMID=pAB510a {ECO:0000313|EMBL:BAI74383.1};
RX PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA Nakayama S., Yamada M., Tabata S., Sato S.;
RT "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT sp. B510.";
RL DNA Res. 17:37-50(2010).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: In the N-terminal section; belongs to the malic enzymes
CC family. {ECO:0000256|ARBA:ARBA00007686}.
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DR EMBL; AP010947; BAI74383.1; -; Genomic_DNA.
DR RefSeq; WP_012976261.1; NC_013855.1.
DR AlphaFoldDB; D3P154; -.
DR KEGG; azl:AZL_a08520; -.
DR HOGENOM; CLU_012366_0_0_5; -.
DR OrthoDB; 9805787at2; -.
DR Proteomes; UP000002040; Plasmid pAB510a.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR CDD; cd05311; NAD_bind_2_malic_enz; 1.
DR Gene3D; 3.40.50.10950; -; 1.
DR Gene3D; 3.40.50.10750; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR015884; Malic_enzyme_CS.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR045213; Malic_NAD-bd_bact_type.
DR InterPro; IPR012188; ME_PTA.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042113; P_AcTrfase_dom1.
DR InterPro; IPR042112; P_AcTrfase_dom2.
DR InterPro; IPR002505; PTA_PTB.
DR PANTHER; PTHR43237; NADP-DEPENDENT MALIC ENZYME; 1.
DR PANTHER; PTHR43237:SF4; NADP-DEPENDENT MALIC ENZYME; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR Pfam; PF01515; PTA_PTB; 1.
DR PIRSF; PIRSF036684; ME_PTA; 1.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00331; MALIC_ENZYMES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036684-2};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|PIRSR:PIRSR036684-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:BAI74383.1}; Plasmid {ECO:0000313|EMBL:BAI74383.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002040}.
FT DOMAIN 18..151
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 163..400
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-1"
FT BINDING 76..83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 136
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-2"
FT BINDING 162
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
FT BINDING 287
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR036684-3"
SQ SEQUENCE 766 AA; 81522 MW; 7309311131276FCE CRC64;
MSGDLKERAL EYHRLGKPGK LAIVPTKPMM TQRDLALAYS PGVAFACTDI VADPANAAEV
TARGNLVAVI SNGTAVLGLG DIGPLASKPV MEGKAVLFKK FADIDVFDIE VDEKDVDALV
DTIARLEPTF GAINLEDIGA PACFEVERRL KERMKIPVFH DDQHGTAIVV AAAVYNALQV
VGKRFEDVRV VSTGGGAAGI ACLDLLVGMG VKRSNIILAD REGVVYQGRN AGMNPYKDRY
ATAGSVRGLD EAMAGADIFL GLSGPGVLTG AMVRTMAARP LILALANPDP EITPEEARAA
RPDAIIATGR SDYPNQVNNV LCFPFIFRGA LDVGATTINE AMKIACVKAI ADMARIEASD
VVAAAYTGEQ LRFGPDYILP KPFDPRLIVD VASAVAQAAM ESGVATRPIA DLRAYRERLG
QYVFRSGLVM KPVFHKAAQA PKRVVYAEGE DERVLRAAQV AVDEGIARPI LLGRDEVVAR
RIEQLGLRLA SGRDVTVVDP VRDPRCHEYA DVYRQVMGRR GVSPNFAATM VRADATVFAS
LMVRRGAADA MVCGTAGRYA EHHRHIRDLL GRRGDAPVSA AMTLLILGKG TYFLTDTHVN
PDPSAEEIAE IAVLAAEKVR HFGIEPKVAL LSHSNFGSSD SPSALKMRAA CELLRRRAPE
LGADGEMQAG AALCEAVRDA ALPNGRLRGQ ANLLVMPTLD AANIALEMLK VLSDGLSVGP
ILLGVSAPAH IVTPEITTRG IVNVTALAVV DAQIDTTPVP LRQAAE
//
